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  • Immunocytochemistry  (2)
  • Directed secretion  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Immunocytochemical localisation of some lysosomal hydrolases, their presence in luminal fluid and their directional secretion by human epididymal cells in culture (1995)
    Springer
    Cell & tissue research 280 (1995), S. 415-425 
    Details
    ISSN: 1432-0878
    Keywords: Epididymis ; Efferent ducts ; Cell culture ; Immunocytochemistry ; Immunoprecipitation ; Man
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The way in which the human epididymis modifies spermatozoa during their sojourn in this structure might be clarified by knowledge of the nature of its secretions. We have examined the presence of several lysosomal hydrolases in human epididymal tissue and fluids, and their synthesis and secretion by monolayer cultures. Tissues were obtained from men undergoing orchidectomy for prostatic carcinoma. The enzymes cathepsin D and acid α-glucosidase were localised in the lysosomes of epithelial cells from the corpus epididymidis, by an immunocytochemical technique. Cathepsin D was also found in epithelial cells of the efferent ducts within lysosomes, apical vesicles and multivesicular bodies. No immunolocalisation of acid glucosidase in the efferent ducts or on the microvilli of the corpus was demonstrable. Cathepsin D, β-hexosaminidase (N-acetylglucosaminidase) and α-glucosidase were measurable in the luminal fluid from the human corpus epididymidis; β-hexosaminidase was secreted into the culture medium by confluent monolayers of epididymal and efferent duct cells. Immunoprecipitation of cell extracts and culture medium of these cultures incubated with 35S-methionine revealed that the precursors of cathepsin D and β-hexosaminidase were synthesized and secreted by such monolayers. Thus, active lytic enzymes are secreted by the human epididymis and could modify sperm membranes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307815
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Immature rat epididymal epithelial cells grown in static primary monolayer culture on permeable supports (1989)
    Springer
    Cell & tissue research 256 (1989), S. 567-572 
    Details
    ISSN: 1432-0878
    Keywords: Epididymis ; Monolayer culture ; Directed secretion ; Phosphatases ; Glucosaminidase ; Rat (Sprague-Dawley)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A cell culture system is characterised for monolayers of immature rat epididymal epithelial cells grown on permeable supports. Cover of the filters was achieved by days 4–5 and was maintained for 9–12 days. The secretion of acid phosphatase (ACP), alkaline phosphatase (AKP) and N-acetylglucosaminidase (NAG) into apical and basal compartments of culture chambers was monitored with time in culture for cells from the proximal and distal epididymis of 37-day-old animals. There was independent secretion of the three enzymes: secretion of NAG and AKP was mainly apical, that of ACP basal; daily secretion of ACP and AKP was constant throughout culture, that of NAG declined; there was greater secretion of NAG and AKP by cells from the proximal than the distal region. The initial high apical secretion of NAG is thought to reflect loss of enzyme from unattached cells, whereas the later AKP secretion is truly directional. Secretion was not influenced by the enzymes used in cell preparation. The cytotoxic agent Thimerosal inhibited secretion of all enzymes when placed beneath the cultures, indicating that secretion depended on viable cells, but initially stimulated release of AKP when applied above the cells possibly reflecting release from the cell membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00225605
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Immunocytochemical localisation of some lysosomal hydrolases, their presence in luminal fluid and their directional secretion by human epididymal cells in culture (1995)
    Springer
    Cell & tissue research 280 (1995), S. 415-425 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Epididymis ; Efferent ducts ; Cell culture ; Immunocytochemistry ; Immunoprecipitation ; Man
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The way in which the human epididymis modifies spermatozoa during their sojourn in this structure might be clarified by knowledge of the nature of its secretions. We have examined the presence of several lysosomal hydrolases in human epididymal tissue and fluids, and their synthesis and secretion by monolayer cultures. Tissues were obtained from men undergoing orchidectomy for prostatic carcinoma. The enzymes cathepsin D and acid α-glucosidase were localised in the lysosomes of epithelial cells from the corpus epididymidis, by an immunocytochemical technique. Cathepsin D was also found in epithelial cells of the efferent ducts within lysosomes, apical vesicles and multivesicular bodies. No immunolocalisation of acid glucosidase in the efferent ducts or on the microvilli of the corpus was demonstrable. Cathepsin D, β-hexosaminidase (N-acetylglucosaminidase) and α-glucosidase were measurable in the luminal fluid from the human corpus epididymidis; β-hexosaminidase was secreted into the culture medium by confluent monolayers of epididymal and efferent duct cells. Immunoprecipitation of cell extracts and culture medium of these cultures incubated with 35S-methionine revealed that the precursors of cathepsin D and β-hexosaminidase were synthesized and secreted by such monolayers. Thus, active lytic enzymes are secreted by the human epididymis and could modify sperm membranes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307815
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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